The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Bacterial lipopolysaccharide induces tyrosine phosphorylation and activation of mitogen-activated protein kinases in macrophages.
Open accessAbstract
Bacterial lipopolysaccharide (LPS) is a potent activator of antibacterial responses by macrophages. Following LPS stimulation, the tyrosine phosphorylation of several proteins is rapidly increased in macrophages, and this event appears to mediate some responses to LPS. We now report that two of these tyrosine phosphoproteins of 41 and 44 kDa are isoforms of mitogen-activated protein (MAP) kinase. Each of these proteins was reactive with anti-MAP kinase antibodies and comigrated with MAP kinase activity in fractions eluted from a MonoQ anion-exchange column. Following LPS stimulation, column fractions containing the tyrosine phosphorylated forms of p41 and p44 exhibited increased MAP kinase activity. Inhibition of LPS-induced tyrosine phosphorylation of these proteins was accompanied by inhibition of MAP kinase activity. Additionally, induction of p41/p44 tyrosine phosphorylation and MAP kinase activity by LPS appeared to be independent of activation of protein kinase C, even though phorbol esters also induced these responses. These results demonstrate that LPS induces the tyrosine phosphorylation and activation of at least two MAP kinase isozymes. Since MAP kinases appear to modulate cellular processes in response to extracellular signals, these kinases may be important targets for LPS action in macrophages.
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“In macrophages and other types of cells, LPS activates three subclasses of MAPKs: extracellular signal-regulated kinase (ERK), c-Jun-terminal kinase (JNK) and p38. Studies have revealed that some compounds are able to suppress proinflammatory cytokines and NF-κB, to inhibit the COX-2 and iNOS expression inhibiting some of these MAPKS [129,130,131].”
From Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review (2010) · cites this paper as [130]
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
CD14, a Receptor for Complexes of Lipopolysaccharide (LPS) and LPS Binding Protein
Wright, S. D., Ramos, R., Tobias, P. S., Ulevitch, R. J., & Mathison, J. C. (1990) · Science · doi:10.1126/science.1698311 · Cited by 3,986
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876
The cell biology of macrophage activation.
Adams, D. O., & Hamilton, T. A. (1984) · Annual Review of Immunology · doi:10.1146/annurev.iy.02.040184.001435 · Cited by 1,628
Phosphorylation of c-jun mediated by MAP kinases
Pulverer, B., Kyriakis, J. M., Avruch, J., Nikolakaki, E., & Woodgett, J. R. (1991) · Nature · doi:10.1038/353670a0 · Cited by 1,470
ENDOTOXINS AND DISEASE MECHANISMS
Morrison, D. C., & Ryan, J. L. (1987) · Annual Review of Medicine · doi:10.1146/annurev.me.38.020187.002221 · Cited by 1,111
Anderson, N. G., Maller, J. L., Tonks, N. K., & Sturgill, T. W. (1990) · Nature · doi:10.1038/343651a0 · Cited by 1,064
Payne, D. M., Rossomando, A. J., Martino, P. A., Erickson, A. K., Her, J. H., Shabanowitz, J., Hunt, D. F., Weber, M. J., & Sturgill, T. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb08021.x · Cited by 1,041
Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
Sturgill, T. W., Ray, L. B., ERIKSON, E., & Maller, J. L. (1988) · Nature · doi:10.1038/334715a0 · Cited by 1,017
Bacterial Endotoxins and Host Immune Responses
Morrison, D. C., & Ryan, J. L. (1980) · Advances in immunology · doi:10.1016/s0065-2776(08)60802-0 · Cited by 606
Ray, L. B., & Sturgill, T. W. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.6.1502 · Cited by 592
Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction.
June, C. H., Fletcher, M. C., Ledbetter, J. A., Schieven, G. L., Siegel, J. N., Phillips, A. F., & Samelson, L. E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.19.7722 · Cited by 491
Extracellular signal-regulated kinases: ERKs in progress.
Cobb, M. H., Boulton, T. G., & Robbins, D. J. (1991) · Cell Regulation · doi:10.1091/mbc.2.12.965 · Cited by 487
Potent selective inhibitors of protein kinase C
Davis, P. D., Hill, C. H., Keech, E., Lawton, G., Nixon, J., Sedgwick, A. D., Wadsworth, J., Westmacott, D., & Wilkinson, S. E. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81494-2 · Cited by 478
Sturgill, T. W., & Wu, J. (1991) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(97)90012-4 · Cited by 430
In vitro effects on microtubule dynamics of purified Xenopus M phase-activated MAP kinase
Gotoh, Y., Nishida, E., Matsuda, S., Shiina, N., Kosako, H., Shiokawa, K., Akiyama, T., Ohta, K., & Sakai, H. (1991) · Nature · doi:10.1038/349251a0 · Cited by 408
Boulton, T. G., & Cobb, M. H. (1991) · Cell Regulation · doi:10.1091/mbc.2.5.357 · Cited by 390
Seger, R., Ahn, N. G., Boulton, T. G., Yancopoulos, G. D., Panayotatos, N., Radziejewska, E., Ericsson, L. H., Bratlien, R. L., Cobb, M. H., & Krebs, E. G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6142 · Cited by 336
Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages.
Weinstein, S. L., Gold, M. R., & DeFranco, A. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4148 · Cited by 311
Self-citation[31] Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases
Uehara, Y., & Fukazawa, H. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)01033-x · Cited by 216
Uehara, Y., Fukazawa, H., Murakami, Y., & Mizuno, S. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92293-6 · Cited by 211
Posada, J. A., Sanghera, J. S., Pelech, S., Aebersold, R. H., & Cooper, J. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2517 · Cited by 199
Self-citationWu, J., Rossomando, A. J., Her, J. H., Vecchio, R., Weber, M. J., & Sturgill, T. W. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.21.9508 · Cited by 137
Sanghera, J. S., Paddon, H. B., Bader, S. A., & Pelech, S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40193-2 · Cited by 134
Self-citationSpecific inhibition of cytoplasmic protein tyrosine kinases by herbimycin A in vitro
Fukazawa, H., Pei-Mlng, L., Yamamoto, C., Murakami, Y., Mizuno, S., & Yoshimasa, U. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90500-5 · Cited by 133
Chung, J., Pelech, S., & Blenis, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4981 · Cited by 119
Self-citationProtein kinase cascades in meiotic and mitotic cell cycle control
Pelech, S., Sanghera, J. S., & Daya‐Makin, M. (1990) · Biochemistry and Cell Biology · doi:10.1139/o90-194 · Cited by 118
Self-citationCrews, C. M., Alessandrini, A., & Erikson, R. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8845 · Cited by 114
Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation
Her, J. H., Wu, J., Rall, T. B., Sturgill, T. W., & Weber, M. J. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.13.3743 · Cited by 93
Sanghera, J. S., Paddon, H. B., & Pelech, S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89555-6 · Cited by 64
Self-citationMajor Substrate for Growth Factor-Activated Protein-Tyrosine Kinases Is a Low-Abundance Protein
Cooper, J. A., & Hunter, T. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.11.3304-3309.1985 · Cited by 54
Research works printed but not linked: 4
- Pabst, 1989, 6, 361
- Barriere, 1991, Patient Care, 25, 95
- Posada, 1991, Mol. Cell Biol., 11, 2517
- Cooper, 1985, Mol. Cell Biol., 5, 3304
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Han, J., Lee, J. D., Bibbs, L., & Ulevitch, R. J. (1994) · Science · doi:10.1126/science.7914033 · Cited by 2,647
Receptor-Dependent Mechanisms of Cell Stimulation by Bacterial Endotoxin
Ulevitch, R. J., & Tobias, P. S. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002253 · Cited by 1,442
Anti-inflammatory Plant Flavonoids and Cellular Action Mechanisms
Kim, H. P., Son, K. H., Chang, H. W., & Kang, S. S. (2004) · Journal of Pharmacological Sciences · doi:10.1254/jphs.crj04003x · Cited by 1,018
Antioxidant and Anti-Inflammatory Activities of Essential Oils: A Short Review
Miguel, M. G. (2010) · Molecules · doi:10.3390/molecules15129252 · Cited by 933
Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Häcker, H., & Wagner, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103217200 · Cited by 805
Metadata
- Authors
- Weinstein, S. L., Sanghera, J. S., Lemke, K., DeFranco, A. L., & Pelech, S. L.
- Affiliations
- University of California, San Francisco (US)
- Genentech (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-07
- Volume
- 267
- Issue
- 21
- Pages
- 14955-14962
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1671728707
- Cited by
- 396
- References
- 31
- Citations by year
- 2026: 2 · 2024: 3 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 5 · 2017: 8 · 2016: 4 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 8
- FWCI
- 8.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI20038)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- lipopolysaccharide, macrophages, tyrosine phosphorylation, mitogen-activated protein kinase, signal transduction, phorbol ester, antibacterial response
- MeSH terms
- Amino Acid Sequence, Animals, Cells, Cultured, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Isoenzymes, Lipopolysaccharides, Macrophages, Molecular Sequence Data, Peptides, Phosphorylation, Precipitin Tests, Protein Kinase C, Protein Kinases, Quinones, Tyrosine, Blotting, Western, Benzoquinones, Rifabutin, Calcium-Calmodulin-Dependent Protein Kinases, Lactams, Macrocyclic, Protein Kinase Inhibitors, Mice
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